dbPTM

KEG_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KEG_ARATH
UniProt AC	Q9FY48
Protein Name	E3 ubiquitin-protein ligase KEG
Gene Name	KEG
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	1625
Subcellular Localization	Golgi apparatus, trans-Golgi network . Early endosome .
Protein Description	Mediates E2-dependent protein ubiquitination. Acts as a negative regulator of abscisic acid signaling. Required for ABI5 degradation, by mediating its ubiquitination. Together with EDR1, may regulate endocytic trafficking and/or the formation of signaling complexes on trans-Golgi network (TGN)/ early endosome (EE) vesicles during stress responses..
Protein Sequence	MVGRVKVPCCSVCHTRYNEDERVPLLLQCGHGFCKDCLSKMFSTSSDTTLTCPRCRHVSVVGNSVQGLRKNYAMLALIHAASGGANFDCDYTDDEDDDDEEDGSDEDGARAARGFHASSSINSLCGPVIEVGAHPEMKLVRQIGEESSSGGFGGVEMWDATVAGGGGRCKHRVAVKKMTLTEDMDVEWMQGQLESLRRASMWCRNVCTFHGVVKMDGSLCLLMDRCFGSVQSEMQRNEGRLTLEQILRYGADVARGVAELHAAGVICMNIKPSNLLLDASGNAVVSDYGLAPILKKPTCQKTRPEFDSSKVTLYTDCVTLSPHYTAPEAWGPVKKLFWEDASGVSPESDAWSFGCTLVEMCTGSTPWDGLSREEIFQAVVKARKVPPQYERIVGVGIPRELWKMIGECLQFKPSKRPTFNAMLATFLRHLQEIPRSPSASPDNGIAKICEVNIVQAPRATNIGVFQDNPNNLHRVVLEGDFEGVRNILAKAAAGGGGSSVRSLLEAQNADGQSALHLACRRGSAELVEAILEYGEANVDIVDKDGDPPLVFALAAGSPQCVHVLIKKGANVRSRLREGSGPSVAHVCSYHGQPDCMRELLVAGADPNAVDDEGETVLHRAVAKKYTDCAIVILENGGSRSMTVSNAKCLTPLHMCVATWNVAVIKRWVEVSSPEEISQAINIPSPVGTALCMAASIRKDHEKEGRELVQILLAAGADPTAQDAQHGRTALHTAAMANNVELVRVILDAGVNANIRNVHNTIPLHMALARGANSCVSLLLESGSDCNIQDDEGDNAFHIAADAAKMIRENLDWLIVMLRSPDAAVDVRNHSGKTVRDFLEALPREWISEDLMEALLKRGVHLSPTIYEVGDWVKFKRGITTPLHGWQGAKPKSVGFVQTILEKEDMIIAFCSGEARVLANEVVKLIPLDRGQHVRLRADVKEPRFGWRGQSRDSVGTVLCVDEDGILRVGFPGASRGWKADPAEMERVEEFKVGDWVRIRQNLTSAKHGFGSVVPGSMGIVYCVRPDSSLLVELSYLPNPWHCEPEEVEPVAPFRIGDRVCVKRSVAEPRYAWGGETHHSVGKISEIENDGLLIIEIPNRPIPWQADPSDMEKIDDFKVGDWVRVKASVSSPKYGWEDITRNSIGVMHSLDEDGDVGIAFCFRSKPFSCSVTDVEKVTPFHVGQEIHMTPSITQPRLGWSNETPATIGKVMRIDMDGTLSAQVTGRQTLWRVSPGDAELLSGFEVGDWVRSKPSLGNRPSYDWSNVGRESIAVVHSIQETGYLELACCFRKGRWSTHYTDLEKIPALKVGQFVHFQKGITEPRWGWRAAKPDSRGIITTVHADGEVRVAFFGLPGLWRGDPADLEVEPMFEVGEWVRLREGVSCWKSVGPGSVGVVHGVGYEGDEWDGTTSVSFCGEQERWAGPTSHLEKAKKLVVGQKTRVKLAVKQPRFGWSGHSHGSVGTISAIDADGKLRIYTPAGSKTWMLDPSEVETIEEEELKIGDWVRVKASITTPTYQWGEVNPSSTGVVHRMEDGDLCVSFCFLDRLWLCKAGELERIRPFRIGDRVKIKDGLVTPRWGWGMETHASKGHVVGVDANGKLRIKFLWREGRPWIGDPADIVLDETSG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
176	Ubiquitination	CKHRVAVKKMTLTED CCCCEEEEECCCCCC	27.39	PubMed
195	Phosphorylation	WMQGQLESLRRASMW HHHHHHHHHHHHHHH	35.45	19880383
436	Phosphorylation	HLQEIPRSPSASPDN HHHHCCCCCCCCCCC	20.18	23776212
438	Phosphorylation	QEIPRSPSASPDNGI HHCCCCCCCCCCCCC	42.50	23776212
440	Phosphorylation	IPRSPSASPDNGIAK CCCCCCCCCCCCCEE	36.80	23776212
974	Phosphorylation	RVGFPGASRGWKADP EEECCCCCCCCCCCH	36.92	30291188

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of KEG_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KEG_ARATH !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of KEG_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ABI5_ARATH	ABI5	physical	17194765
ABI5_ARATH	ABI5	physical	20682837
EDR1_ARATH	EDR1	physical	21343429
KEG_ARATH	KEG	physical	21343429
AI5L4_ARATH	ABF1	physical	23742014
AI5L6_ARATH	ABF3	physical	23742014
UBC8_ARATH	UBC8	physical	23742014
SDE3_ARATH	SDE3	physical	26320228
IF62_ARATH	emb1624	physical	26320228
CIPKQ_ARATH	AT5G21326	physical	26320228
FDH_ARATH	FDH	physical	29270890
CIPK3_ARATH	CIPK3	physical	29270890

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of KEG_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks."; Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.; Plant Physiol. 150:889-903(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-974, AND MASSSPECTROMETRY.	19376835 [Abstract]